Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2003-12-23
pubmed:abstractText
Engagement of integrin receptors with the extracellular matrix induces the formation of focal adhesions (FAs). Dynamic regulation of FAs is necessary for cells to polarize and migrate. Key interactions between FA scaffolding and signaling proteins are dependent on tyrosine phosphorylation. However, the precise role of tyrosine phosphorylation in FA development and maturation is poorly defined. Here, we show that phosphorylation of type Igamma phosphatidylinositol phosphate kinase (PIPKIgamma661) on tyrosine 644 (Y644) is critical for its interaction with talin, and consequently, localization to FAs. PIPKIgamma661 is specifically phosphorylated on Y644 by Src. Phosphorylation is regulated by focal adhesion kinase, which enhances the association between PIPKIgamma661 and Src. The phosphorylation of Y644 results in an approximately 15-fold increase in binding affinity to the talin head domain and blocks beta-integrin binding to talin. This defines a novel phosphotyrosine-binding site on the talin F3 domain and a "molecular switch" for talin binding between PIPKIgamma661 and beta-integrin that may regulate dynamic FA turnover.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-10497155, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-10512882, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-10559917, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11082272, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11114741, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11259684, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11279249, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11493667, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11544027, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11707509, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11715046, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11779709, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11932255, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-11994743, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-12213832, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-12422219, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-12422220, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-12535520, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-12782621, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-12846579, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-12867986, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-12894175, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-14526080, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-1943760, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-2468126, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-2476666, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-3011478, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-8387531, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-8970735, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-9497328, http://linkedlifedata.com/resource/pubmed/commentcorrection/14691141-9889179
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1-phosphatidylinositol-4-phosphate..., http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Kinase 1, http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Protein-Tyrosine..., http://linkedlifedata.com/resource/pubmed/chemical/Integrin beta Chains, http://linkedlifedata.com/resource/pubmed/chemical/PTK2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group..., http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Ptk2 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Talin, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine, http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
163
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1339-49
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:14691141-Amino Acid Sequence, pubmed-meshheading:14691141-Animals, pubmed-meshheading:14691141-Binding Sites, pubmed-meshheading:14691141-Cell Membrane, pubmed-meshheading:14691141-Chick Embryo, pubmed-meshheading:14691141-Focal Adhesion Kinase 1, pubmed-meshheading:14691141-Focal Adhesion Protein-Tyrosine Kinases, pubmed-meshheading:14691141-Focal Adhesions, pubmed-meshheading:14691141-Humans, pubmed-meshheading:14691141-Integrin beta Chains, pubmed-meshheading:14691141-Phosphorylation, pubmed-meshheading:14691141-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:14691141-Protein Binding, pubmed-meshheading:14691141-Protein Structure, Tertiary, pubmed-meshheading:14691141-Protein-Tyrosine Kinases, pubmed-meshheading:14691141-Rats, pubmed-meshheading:14691141-Talin, pubmed-meshheading:14691141-Tyrosine, pubmed-meshheading:14691141-src-Family Kinases
pubmed:year
2003
pubmed:articleTitle
Tyrosine phosphorylation of type Igamma phosphatidylinositol phosphate kinase by Src regulates an integrin-talin switch.
pubmed:affiliation
Department of Pharmacology, Program in Molecular and Cellular Pharmacology, University of Wisconsin Medical School, Madison, WI 53706, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't